Asked by Reba
A protein molecule in its folded native state has one favored conformation, but when it is denatured it becomes a random coil, with very many possible conformations.
What must be the sign of the change in entropy (S) for the change native---> denatured
Would this be positive, since the protein is becoming more disordered?
Will the contribution of the change in S to the free energy change be positive or negative?
Would this be negative since a negative change in G indicates a spontaneous reaction, hence more disorder?
What requirement does this impose if proteins are to be stable structures?
I'm not sure about this answer
What must be the sign of the change in entropy (S) for the change native---> denatured
Would this be positive, since the protein is becoming more disordered?
Will the contribution of the change in S to the free energy change be positive or negative?
Would this be negative since a negative change in G indicates a spontaneous reaction, hence more disorder?
What requirement does this impose if proteins are to be stable structures?
I'm not sure about this answer
Answers
Answered by
DrBob222
I think your answer to #1 is correct.
I think your answer to #2 is correct but I don't necessarily agree with your wording. I think the delta S indicates a more negative free energy; I don't know that I agree with the reverse of that.
I think the answer to #3 is that the protein must not be denatured (must remain in its native state).
I think your answer to #2 is correct but I don't necessarily agree with your wording. I think the delta S indicates a more negative free energy; I don't know that I agree with the reverse of that.
I think the answer to #3 is that the protein must not be denatured (must remain in its native state).
There are no AI answers yet. The ability to request AI answers is coming soon!